Respiratory Flashcards

1
Q

name the four types of hypoxia

A

Hypoxic hypoxia
anaemic hypoxia
Stagnant hypoxia
histotoxic hypoxia

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2
Q

What are west zones

A

the lung is divided into 3 zones
in Zone1 PA>Pa>Pv - zone is poorly perfused and little gas exchange takes place
in zone 2 Pa>PA>Pv - represents bulk of lung in healthy people
in the zone 3 Pa>Pv>PA - flow is proportional to gradient between pulmonary arterial and pulmonary venous pressure

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3
Q

What is the effect of IPPV on west zones

A

Increased alveolar pressure due to IPPV can push blood out of the lung creating a zone 1

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4
Q

What is dead space

A

Dead space is an area of the lung which is ventilated but not perfused so the gas doesnt not take part in gas exchange therefore v/q = 1/0 resulting in infinity
e.g PE

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5
Q

What is shunt

A

Shunt is an area of the lung that is perfused but not ventilated e.g. in pneumonia or pulmonary oedema
v/q = 0/1 therefore 0

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6
Q

What is closing capacity

A

Closing capacity is the volume at which the smallest airways (respiratory bronchioles) begin to close
it is a sum of closing volume and residual volume

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7
Q

What is the difference between closing capacity and closing volume

A

Closing volumes is part of closing capacity
CV is when the small airways begin to close in the dependent areas of the lung

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8
Q

What factors increase closing capacity

A

Age
chronic bronchitis
Smoking
LV failure
Surgery

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9
Q

What is the relationship between closing capacity and FRC

A

CC is approx half of FRC when upright and 2/3 of FRC when supine
If cc exceeds FRC the small airways will close prematurely resulting in impaired gas exchange

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10
Q

What is the alveolar gas equation?

A

Pa02 = FiO2(Patm -PH20) - PaCO2/RQ

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11
Q

How does preoxygenation improve Pa02

A

Pre oxygenation is giving a patient oxygen prior to intubation to extend safe apnoea time
It improves PaO2 by denitrogenating the lungs
if look at alveolar gas equation with 0.21 and 1.0 causes and increase in PaO2
causes an increase in oxygen reserve
oxygen consumption during apnoea is around 200-250ml/min

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12
Q

What are the functions of FRC

A

FRC is the volume of gas remaining in the lungs after passive expiration
Acts as an oxygen reserve to maintain oxygenation between breaths

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13
Q

what is surfactant

A

Surface-active complex of phospholipids and proteins formed by type II alveolar cells.
main lipid component of the surfactant, dipalmitoylphosphatidylcholine (DPPC), reduces surface tension.

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14
Q

How is O2 transported in the body

A

99% of oxygen is carried bound to haemoglobin and 1% dissolved in solution
Oxygen content is 200ml/L at 97% sats

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15
Q

In what ways is CO2 transported in the body

A

20times more soluble in blood than oxygen. Carried in three different forms
- dissolved
- bicarbonate
- carbamino compounds

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16
Q

how do we calculate oxygen content in the blood

A

CaO2 = 1.34 x Hb x Sats + (0.0225 x PaO2)
1.34 is huffners constant

17
Q

What are the different forms of haemoglobin

A

HbA - consists of 2 alpha chains and 2 beta chains
HbF - foetal Hb contains 2 alpha and 2 gamma
hbA2 - 2-3% of population contains 2 alpha and 2 delta chains

18
Q

What is the p50 on the oxyhaemoglobin dissociation curve

A

The partial pressure of oxygen in the blood at which hb is 50% saturated (kPa) - usually around 3.5kPa

19
Q

What causes a left shift of the curve/for the p50 to decrease

A

Decreased PaCO2
alkalosis
decreased temp
decreased 2,3DPG
fetal Hb
CO
Methaemoglobin
*increased affinity for oxygen

20
Q

what causes the oxyhaemoglobin dissociation curve to shift to the right

A

*decreased affinity for oxygen
increased temp
increased paCO2
increased 2,3 DPG
pregnancy
Altitude
Acidosis

21
Q

What is the PaO2 in the arterial blood

A

13.3kPa at 100% sats

22
Q

What is the Pao2 in the venous blood

A

5.3kPa at 75% sats

23
Q

How are RBC produced

A

the process of rbc production is called erythropoiesis.
Production of rbcs is controlled by erythropoietin, a hormone produced in the kidneys.
rbcs start as immature cells in the red bone marrow and after about seven days of maturation they are released into the bloodstream. the stages of rbc formation are:
Proerythroblast → Prorubricyte → Rubricyte → normoblast → Reticulocyte (nucleus ejected by this phase, allowing the centre of the cell to indent giving the cell its biconcave shape – these now squeeze out of the bone marrow and into the circulation) → erythroblast
Hypoxia (e.g. altitude or anaemia) stimulates the kidney to release more erythropoietin, which acts on the red bone marrow where it increases the speed of reticulocyte formation.

24
Q

How are RBCs removed from circulation

A

rbcs survive for about 120 days. their cell membranes are exposed to a lot of wear and tear as they squeeze through blood capillaries. without a nucleus and other organelles, rbcs cannot synthesise new components. worn out rbcs are removed from the circulation and destroyed by fixed phagocytic macrophages in the spleen and the liver and the breakdown products are recycled.

25
What happens to the breakdown products of RBC
Haemoglobin gets split into its haem and globin components – the globin is broken down into amino acids and the haem gets broken down into iron and biliverdin. the iron combines with the plasma protein transferrin, which transports the iron in the bloodstream. in the muscle, liver and spleen, iron detaches from transferrin and combines with iron-storing proteins – ferritin and haemosiderin. when iron is released from its storage site or absorbed from the gut, it combines with transferrin and gets transported to the bone marrow where it is used for rbc production. biliverdin gets converted into bilirubin, which enters the circulation and is transported to the liver where it is secreted into the bile.
26
Why is haemoglobin essential
oxygen is relatively insoluble in water and therefore only approximately 1.5% of total oxygen is carried dissolved in the plasma. the remaining 98.5% is bound to haemoglobin. Haemoglobin increases the oxygen-carrying capacity of blood approximately 70-fold.
27
Describe the molecular structure of Haemoglobin
Haemoglobin group is a tetrameter composed of 4 subunits Each subunit contains a polypeptide chain in association with a haem group. Haem group consists of a central charged iron atom held in a ring structure called porphyrin. 98% of adult haemoglobin is HBA1 which has 2 alpha chains and 2 beta chains HbA2 has 2 alpha chains and 2 delta chains HbF has 2 alpha and 2 gamma chains. HbF changes to HbA around 6 months of life
28
What happens to haemoglobin in sickle cell anaemia
sickle cell anaemia is an inherited autosomal recessive blood disorder in which there is an abnormal β polypeptide chain due to a genetic mutation in the amino acid sequence where the amino acid valine is replaced by glutamic acid. in the heterozygous state this confers an advantage against malaria as the shortened lifespan of the erythrocyte prevents the blood-borne phase of the mosquito from completing its life cycle. in the homozygous state the abnormal haemoglobin is susceptible to forming solid, non-pliable sickle-like structures when exposed to low Pao2, causing the erythrocytes to obstruct the microcirculation, leading to painful crises and infarcts.
29
What happens to haemoglobin in thalassaemia
thalassaemia is an inherited autosomal recessive blood disorder in which the genetic defect results in a reduced rate of synthesis of one of the globin chains that make up haemoglobin. this can result in the formation of abnormal haemoglobin molecules, causing anaemia. thalassaemia can be α or β depending on which globin chain is being underproduced. thalassaemia is a quantitative problem where too few globin chains are synthesised, whereas sickle cell anaemia is a qualitative problem with the synthesis of an incorrectly functioning globin chain.
30
How does oxygen bind to haemoglobin
oxygen binds to the ferrous iron (Fe2+) in haemoglobin by forming a reversible bond. there is no oxidative reaction and so the iron atom always remains in the ferrous form. in the condition methaemoglobinaemia, the ferrous iron is oxidised into the ferric (Fe3+) form. each molecule of haemoglobin can bind four molecules of oxygen (i.e. one at each ferrous ion within each haem group). there are several factors that influence binding including local oxygen tension, local tissue environment (temperature, co2, hydrogen ions and 2,3 dPg) and the allosteric change and cooperative binding behaviour of oxygen to haemoglobin (see chapter 2, ‘oxygen–haemoglobin dissociation curve’, for further details).
31
Can the dissolved fraction of oxygen be dismissed
even though dissolved oxygen represents a small fraction of total oxygen- carrying capacity of the blood, it still constitutes an important fraction. severe anaemia illustrates the point, e.g. for a Jehovah’s witness who has experienced a massive intra-operative haemorrhage and refuses blood transfusion. one therapeutic option would be the use of hyperbaric oxygen therapy; at three atmospheres and using 100% oxygen the dissolved fraction of oxygen would meet total body oxygen requirements. the dissolved fraction of oxygen is also responsible for triggering the hypoxic respiratory drive. this is of clinical significance in patients with coPd who are chronic co2 retainers, because giving them high-flow oxygen to increase their Pao2 may lead to loss of their hypoxic drive. in 2008, the british thoracic society published guidelines on the use of emergency oxygen in adults. the guidelines recommend that oxygen be administered to patients whose oxygen saturations fall below the target range (94–98% for most acutely ill patients and 88–92% for those at risk of type 2 respiratory failure with raised co2 levels in the blood).
32
What is the bohr effect
Refers to the right shift in the oxygen dissociation curve which is in response to decreased pH, increased PaCO2 or increased temp. decreased oxygen affinity at low ph or high paco2 - facilitates release at tissues
33
What is the double bohr effect
this refers to the situation in the placenta where the bohr effect operates in both the maternal and fetal circulations. the increase in Pco2 in the maternal intervillous sinuses assists oxygen unloading. the decrease in Pco2 on the fetal side of the circulation assists oxygen loading. the bohr effect facilitates the reciprocal exchange of oxygen for carbon dioxide. the double bohr effect means that the oxygen dissociation curves for maternal Hba and fetal HbF move apart − i.e. right shift (maternal); left shift (fetal).
34
What is the Haldane effect
the Haldane effect describes the ability of hemoglobin to carry increased amounts of carbon dioxide (CO2) in the deoxygenated state as opposed to the oxygenated state. facilitates removal of co2 from the tissues
35
What does the myoglobin dissociation curve look like
rectangular hyperbola also lies to the left of the OHDC due to myoglobin having a higher affinity for oxygen than haemoglobin
36